Web Release Date: May 11,
Identification of N-Linked Glycoproteins in Human Saliva by Glycoprotein Capture and Mass Spectrometry
and
Department of Chemistry and Biochemistry, UCLA School of Dentistry and UCLA Dental Research Institute, and Department of Biological Chemistry, David Geffen School of Medicine, University of California-Los Angeles, Los Angeles, California
Received December 31, 2005
Abstract:
Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity. Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body. Salivary glycoproteins were identified by the hydrazide coupling and release method. In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS. Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins. Of these, 16 glycoproteins have not been reported previously in saliva. In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
Keywords: glycoproteins 
tandem mass spectrometry salivary
proteins 2D gel electrophoresis mucin solution isoelectric
focusing
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